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Conserved domains on  [gi|17552228|ref|NP_497827|]
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Glyoxalase 1 [Caenorhabditis elegans]

Protein Classification

VOC family protein( domain architecture ID 11675439)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to Homo sapiens glyoxalase domain-containing protein 4

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
3-127 9.80e-80

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


The actual alignment was detected with superfamily member cd08358:

Pssm-ID: 472697  Cd Length: 127  Bit Score: 236.88  E-value: 9.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   3 ARALHYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGCEATCNGPYNGRWSKTMIGYGSEDEHFVLEITYNYPIHKYELG 82
Cdd:cd08358   1 RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17552228  83 NDYRAIVIDSDQLFEKVEKINHRKSGCGR--LAVKDPDGHEFKIGKA 127
Cdd:cd08358  81 NDFLGITIHSKQAVSRAKKHNWPVTQVGDgvYEVKAPGGYKFYLIDK 127
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
135-248 5.07e-61

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


:

Pssm-ID: 319964  Cd Length: 114  Bit Score: 188.53  E-value: 5.07e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 135 RVQVNVGDLEKSKKYWNETLGMPIVEEKSSRIRMSYGDGQCELEIVKSQDKIDRKTGFGRIAFSYPEDKLESLQDKIKSA 214
Cdd:cd16357   1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVKAA 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 17552228 215 NGTIINELTTLETPGKADVQVVILADPDEHEICF 248
Cdd:cd16357  81 GQTILTPLVSLDTPGKATVQVVILADPDGHEICF 114
 
Name Accession Description Interval E-value
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
3-127 9.80e-80

N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319946  Cd Length: 127  Bit Score: 236.88  E-value: 9.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   3 ARALHYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGCEATCNGPYNGRWSKTMIGYGSEDEHFVLEITYNYPIHKYELG 82
Cdd:cd08358   1 RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17552228  83 NDYRAIVIDSDQLFEKVEKINHRKSGCGR--LAVKDPDGHEFKIGKA 127
Cdd:cd08358  81 NDFLGITIHSKQAVSRAKKHNWPVTQVGDgvYEVKAPGGYKFYLIDK 127
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
135-248 5.07e-61

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319964  Cd Length: 114  Bit Score: 188.53  E-value: 5.07e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 135 RVQVNVGDLEKSKKYWNETLGMPIVEEKSSRIRMSYGDGQCELEIVKSQDKIDRKTGFGRIAFSYPEDKLESLQDKIKSA 214
Cdd:cd16357   1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVKAA 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 17552228 215 NGTIINELTTLETPGKADVQVVILADPDEHEICF 248
Cdd:cd16357  81 GQTILTPLVSLDTPGKATVQVVILADPDGHEICF 114
PLN02300 PLN02300
lactoylglutathione lyase
4-254 3.41e-27

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 106.79  E-value: 3.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228    4 RALHYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGceatcngpyngRWSKTMIGYGSEDEHFVLEITYNYPIHKYELGN 83
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEE-----------KYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   84 DYRAIVIDSDQLFEKVEKInhrKSGCGRLA---------------VKDPDGHEFKIGKADQSPKVL-RVQVNVGDLEKSK 147
Cdd:PLN02300  93 GFGHFGIAVEDVAKTVELV---KAKGGKVTrepgpvkggksviafVKDPDGYKFELIQRGPTPEPLcQVMLRVGDLDRSI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228  148 KYWNETLGMPIV------EEKSSRIRMSYG--DGQCELEIVKSQD--KIDRKTGFGRIAFSypEDKLESLQDKIKSANGT 217
Cdd:PLN02300 170 KFYEKAFGMKLLrkrdnpEYKYTIAMMGYGpeDKTTVLELTYNYGvtEYTKGNAYAQIAIG--TDDVYKTAEAIKLVGGK 247
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 17552228  218 IINELTTLetPGkADVQVVILADPDEHEICFVGDEGF 254
Cdd:PLN02300 248 ITREPGPL--PG-INTKITACLDPDGWKTVFVDNIDF 281
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
4-124 4.30e-21

lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other]


Pssm-ID: 272886  Cd Length: 150  Bit Score: 86.78  E-value: 4.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228     4 RALHYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGceatcngpyngRWSKTMIGYGSEDEHFVLEITYNYPIHKYELGN 83
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEM-----------KFSLAFLGYGDETSAAVIELTHNWGTEKYDLGN 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17552228    84 DYRAIVIDSDQLFEKVEKINHR-----------KSGCGRLA-VKDPDGHEFKI 124
Cdd:TIGR00068  86 GFGHIAIGVDDVYKACERVRALggnvvrepgpvKGGTTVIAfVEDPDGYKIEL 138
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
132-248 1.85e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 60.15  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   132 KVLRVQVNVGDLEKSKKYWNETLGMPIVE-----EKSSRIRMSYGDGQCELEIVKSQDKIDRKTGFGR--IAFSYPE-DK 203
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEetdagEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGhhIAFIAFSvDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 17552228   204 LESLQDKIKSANGTIINELTTletpGKADVQVVILADPDEHEICF 248
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGR----HGWGGRYSYFRDPDGNLIEL 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
136-249 3.73e-09

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 53.84  E-value: 3.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 136 VQVNVGDLEKSKKYWNETLGMPIVEE------KSSRIRMSYGDGQcELEIVKSQD--KIDRKTGFGRIAFSYPEdkLESL 207
Cdd:COG0346   6 VTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLGDGT-ELELFEAPGaaPAPGGGGLHHLAFRVDD--LDAA 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17552228 208 QDKIKSANGTIINElttlETPGKADVQVVILADPDEHEICFV 249
Cdd:COG0346  83 YARLRAAGVEIEGE----PRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-122 4.43e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 47.83  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228     7 HYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGceatcngpyngrwsKTMIGYGSEDEHFVLEITYNYPIHKYELGNDYR 86
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE--------------GGLRSAFFLAGGRVLELLLNETPPPAAAGFGGH 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 17552228    87 ---AIVIDSDQLFEKVEKI-----------NHRKSGCGRLAVKDPDGHEF 122
Cdd:pfam00903  70 hiaFIAFSVDDVDAAYDRLkaagveivrepGRHGWGGRYSYFRDPDGNLI 119
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
7-120 3.42e-06

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 45.37  E-value: 3.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   7 HYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGceatcngpyngrwSKTMIGYGSEDEHfVLEITYNYPIHKYELGNDYR 86
Cdd:COG0346   5 HVTLRVSDLEASLAFYTDVLGLELVKRTDFGDG-------------GFGHAFLRLGDGT-ELELFEAPGAAPAPGGGGLH 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17552228  87 --AIVIDS-DQLFEK--------VEKINHRKSGCGRLAVKDPDGH 120
Cdd:COG0346  71 hlAFRVDDlDAAYARlraagveiEGEPRDRAYGYRSAYFRDPDGN 115
 
Name Accession Description Interval E-value
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
3-127 9.80e-80

N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319946  Cd Length: 127  Bit Score: 236.88  E-value: 9.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   3 ARALHYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGCEATCNGPYNGRWSKTMIGYGSEDEHFVLEITYNYPIHKYELG 82
Cdd:cd08358   1 RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17552228  83 NDYRAIVIDSDQLFEKVEKINHRKSGCGR--LAVKDPDGHEFKIGKA 127
Cdd:cd08358  81 NDFLGITIHSKQAVSRAKKHNWPVTQVGDgvYEVKAPGGYKFYLIDK 127
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
135-248 5.07e-61

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319964  Cd Length: 114  Bit Score: 188.53  E-value: 5.07e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 135 RVQVNVGDLEKSKKYWNETLGMPIVEEKSSRIRMSYGDGQCELEIVKSQDKIDRKTGFGRIAFSYPEDKLESLQDKIKSA 214
Cdd:cd16357   1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVKAA 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 17552228 215 NGTIINELTTLETPGKADVQVVILADPDEHEICF 248
Cdd:cd16357  81 GQTILTPLVSLDTPGKATVQVVILADPDGHEICF 114
PLN02300 PLN02300
lactoylglutathione lyase
4-254 3.41e-27

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 106.79  E-value: 3.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228    4 RALHYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGceatcngpyngRWSKTMIGYGSEDEHFVLEITYNYPIHKYELGN 83
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEE-----------KYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   84 DYRAIVIDSDQLFEKVEKInhrKSGCGRLA---------------VKDPDGHEFKIGKADQSPKVL-RVQVNVGDLEKSK 147
Cdd:PLN02300  93 GFGHFGIAVEDVAKTVELV---KAKGGKVTrepgpvkggksviafVKDPDGYKFELIQRGPTPEPLcQVMLRVGDLDRSI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228  148 KYWNETLGMPIV------EEKSSRIRMSYG--DGQCELEIVKSQD--KIDRKTGFGRIAFSypEDKLESLQDKIKSANGT 217
Cdd:PLN02300 170 KFYEKAFGMKLLrkrdnpEYKYTIAMMGYGpeDKTTVLELTYNYGvtEYTKGNAYAQIAIG--TDDVYKTAEAIKLVGGK 247
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 17552228  218 IINELTTLetPGkADVQVVILADPDEHEICFVGDEGF 254
Cdd:PLN02300 248 ITREPGPL--PG-INTKITACLDPDGWKTVFVDNIDF 281
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
4-124 4.30e-21

lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other]


Pssm-ID: 272886  Cd Length: 150  Bit Score: 86.78  E-value: 4.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228     4 RALHYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGceatcngpyngRWSKTMIGYGSEDEHFVLEITYNYPIHKYELGN 83
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEM-----------KFSLAFLGYGDETSAAVIELTHNWGTEKYDLGN 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17552228    84 DYRAIVIDSDQLFEKVEKINHR-----------KSGCGRLA-VKDPDGHEFKI 124
Cdd:TIGR00068  86 GFGHIAIGVDDVYKACERVRALggnvvrepgpvKGGTTVIAfVEDPDGYKIEL 138
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
6-124 1.30e-20

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 84.76  E-value: 1.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   6 LHYVFKVANRAKTIDFFTNVLNMKVLRHEEFEkgceatcngpyNGRWSKTMIGYGSEDEHFVLEITYNYPIHKYELGNDY 85
Cdd:cd16358   2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYP-----------EGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAY 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17552228  86 RAIVIDSDQLFEKVEKINHR-----------KSGCGRLA-VKDPDGHEFKI 124
Cdd:cd16358  71 GHIAIGVEDVYETCERIRKKggkvtrepgpmKGGTTVIAfVEDPDGYKIEL 121
PRK10291 PRK10291
glyoxalase I; Provisional
9-134 5.33e-15

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 70.05  E-value: 5.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228    9 VFKVANRAKTIDFFTNVLNMKVLRHEEfekgceatcNGPYngRWSKTMIGYGSEDEHFVLEITYNYPIHKYELGNDYRAI 88
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSE---------NPEY--KYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHI 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17552228   89 VIDSDQLFEKVEKINHRKSGCGRLA------------VKDPDGHEFKIGKADQSPKVL 134
Cdd:PRK10291  70 ALSVDNAAEACEKIRQNGGNVTREAgpvkggttviafVEDPDGYKIELIEEKDAGRGL 127
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
132-248 1.85e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 60.15  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   132 KVLRVQVNVGDLEKSKKYWNETLGMPIVE-----EKSSRIRMSYGDGQCELEIVKSQDKIDRKTGFGR--IAFSYPE-DK 203
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEetdagEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGhhIAFIAFSvDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 17552228   204 LESLQDKIKSANGTIINELTTletpGKADVQVVILADPDEHEICF 248
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGR----HGWGGRYSYFRDPDGNLIEL 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
136-249 3.73e-09

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 53.84  E-value: 3.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 136 VQVNVGDLEKSKKYWNETLGMPIVEE------KSSRIRMSYGDGQcELEIVKSQD--KIDRKTGFGRIAFSYPEdkLESL 207
Cdd:COG0346   6 VTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLGDGT-ELELFEAPGaaPAPGGGGLHHLAFRVDD--LDAA 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17552228 208 QDKIKSANGTIINElttlETPGKADVQVVILADPDEHEICFV 249
Cdd:COG0346  83 YARLRAAGVEIEGE----PRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-122 4.43e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 47.83  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228     7 HYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGceatcngpyngrwsKTMIGYGSEDEHFVLEITYNYPIHKYELGNDYR 86
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE--------------GGLRSAFFLAGGRVLELLLNETPPPAAAGFGGH 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 17552228    87 ---AIVIDSDQLFEKVEKI-----------NHRKSGCGRLAVKDPDGHEF 122
Cdd:pfam00903  70 hiaFIAFSVDDVDAAYDRLkaagveivrepGRHGWGGRYSYFRDPDGNLI 119
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
136-252 8.53e-07

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 47.26  E-value: 8.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 136 VQVNVGDLEKSKKYWNETLGMPIVEEKSSRIRMSYGDGQCELEIVKSQDKIDRK--TGFGRIAFSYP-EDKLESLQDKIK 212
Cdd:COG2514   7 VTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAPPRPgaAGLDHVAFRVPsRADLDAALARLA 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17552228 213 SANgtiinelttLETPGKADVQV---VILADPDEHEICFVGDE 252
Cdd:COG2514  87 AAG---------VPVEGAVDHGVgesLYFRDPDGNLIELYTDR 120
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
7-120 3.42e-06

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 45.37  E-value: 3.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   7 HYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGceatcngpyngrwSKTMIGYGSEDEHfVLEITYNYPIHKYELGNDYR 86
Cdd:COG0346   5 HVTLRVSDLEASLAFYTDVLGLELVKRTDFGDG-------------GFGHAFLRLGDGT-ELELFEAPGAAPAPGGGGLH 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17552228  87 --AIVIDS-DQLFEK--------VEKINHRKSGCGRLAVKDPDGH 120
Cdd:COG0346  71 hlAFRVDDlDAAYARlraagveiEGEPRDRAYGYRSAYFRDPDGN 115
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
136-248 5.06e-06

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 44.44  E-value: 5.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 136 VQVNVGDLEKSKKYWNETLGMPIVEEKSSR--IRMSYGDGQCeLEIVKSQDKIDRK-TGFGRIAFSypEDKLESLQDKIK 212
Cdd:cd06587   2 VALRVPDLDASVAFYEEVLGFEVVSRNEGGgfAFLRLGPGLR-LALLEGPEPERPGgGGLFHLAFE--VDDVDEVDERLR 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17552228 213 SANGTIINELTTLETPGkaDVQVVILADPDEHEICF 248
Cdd:cd06587  79 EAGAEGELVAPPVDDPW--GGRSFYFRDPDGNLIEF 112
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
7-119 9.66e-05

Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 41.54  E-value: 9.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   7 HYVFKVANRAKTIDFFTNVLNMKVLRHEEFEK--------GCEATCNGPYNGRWSKTMigygseDEHFVLEITYNY---- 74
Cdd:cd07233   3 HTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEmkfslyflGYEDPKDIPKDPRTAWVF------SREGTLELTHNWgten 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228  75 -PIHKYELGNDYR------AI-VIDSDQLFEKVEKIN---HRKSGCGR---LA-VKDPDG 119
Cdd:cd07233  77 dEDPVYHNGNSDPrgfghiGIaVDDVYAACERFEELGvkfKKKPDDGKmkgIAfIKDPDG 136
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
132-249 1.88e-04

Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only];


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 40.39  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 132 KVLRVQVNVGDLEKSKKYWNETLGMPIVEEKSSRIRM---SYGDGQcELEIVKSQDkiDRKTGFGRIAFsYPEDkLESLQ 208
Cdd:COG3324   4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYaefDTDGGQ-VGGLMPGAE--EPGGPGWLLYF-AVDD-LDAAV 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17552228 209 DKIKSANGTIINELTTLETPGKadvqVVILADPDEHEICFV 249
Cdd:COG3324  79 ARVEAAGGTVLRPPTDIPPWGR----FAVFRDPEGNRFGLW 115
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
133-249 2.10e-04

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 40.07  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228 133 VLRVQVNVGDLEKSKKYWNETLGMP------IVEEKSSRIRMSYGDGQ----CELEIVKSQDKIDRKTGFGRIAFSYpeD 202
Cdd:cd16358   1 MLHTMLRVGDLDRSIKFYTEVLGMKllrkrdYPEGKYTLAFVGYGDEDentvLELTYNWGVDKYDLGTAYGHIAIGV--E 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17552228 203 KLESLQDKIKSANGTIINElttletPGKADVQVVILA---DPDEHEICFV 249
Cdd:cd16358  79 DVYETCERIRKKGGKVTRE------PGPMKGGTTVIAfveDPDGYKIELI 122
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
7-124 3.77e-04

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 39.43  E-value: 3.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552228   7 HYVFKVANRAKTIDFFTNVLNMKVLRHEEFEKGCEATCNGpyngrwsktmigygsedeHFVLEITYNYPiHKYELGNDYR 86
Cdd:cd06587   1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGP------------------GLRLALLEGPE-PERPGGGGLF 61
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17552228  87 AI---VIDSDQLFEK----------VEKINHRKSGCGRLAVKDPDGHEFKI 124
Cdd:cd06587  62 HLafeVDDVDEVDERlreagaegelVAPPVDDPWGGRSFYFRDPDGNLIEF 112
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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